4dwh

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dwh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DWH FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dwh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DWH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwh OCA], [https://pdbe.org/4dwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dwh RCSB], [https://www.ebi.ac.uk/pdbsum/4dwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dwh ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwh OCA], [https://pdbe.org/4dwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dwh RCSB], [https://www.ebi.ac.uk/pdbsum/4dwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dwh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FIMC_ECOLI FIMC_ECOLI]] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.
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[https://www.uniprot.org/uniprot/FIMC_ECOLI FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Type 1 pili from uropathogenic Escherichia coli are filamentous, noncovalent protein complexes mediating bacterial adhesion to the host tissue. All structural pilus subunits are homologous proteins sharing an invariant disulfide bridge. Here we show that disulfide bond formation in the unfolded subunits, catalyzed by the periplasmic oxidoreductase DsbA, is required for subunit recognition by the assembly chaperone FimC and for FimC-catalyzed subunit folding. FimC thus guarantees quantitative disulfide bond formation in each of the up to 3,000 subunits of the pilus. The X-ray structure of the complex between FimC and the main pilus subunit FimA and the kinetics of FimC-catalyzed FimA folding indicate that FimC accelerates folding of pilus subunits by lowering their topological complexity. The kinetic data, together with the measured in vivo concentrations of DsbA and FimC, predict an in vivo half-life of 2 s for oxidative folding of FimA in the periplasm.
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Quality control of disulfide bond formation in pilus subunits by the chaperone FimC.,Crespo MD, Puorger C, Scharer MA, Eidam O, Grutter MG, Capitani G, Glockshuber R Nat Chem Biol. 2012 Jul 1. doi: 10.1038/nchembio.1019. PMID:22772153<ref>PMID:22772153</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4dwh" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Pilin 3D structures|Pilin 3D structures]]
*[[Pilin 3D structures|Pilin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 14:46, 14 March 2024

Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution)

PDB ID 4dwh

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